Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193

α-Amylases are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. In this study, a novel gene encoding α-amylase was cloned from marine bacterium Salinispora arenicola CNP193 and the protein was expressed in Escherichia coli. The α-amylase gene from S. arenicola CNP193 had a length of 1839 bp and encoded a α-amylase with an estimated molecular mass of 74 kDa. The optimum temperature and pH for the recombinant α-amylase was 50 °C and 7 respectively. Na⁺, K⁺ and Ca²⁺ increased the activity of the recombinant α-amylase whereas the enzyme was inhibited by Cu²⁺, Zn²⁺, Hg²⁺, Pb²⁺, Fe³⁺ and Mn²⁺. Thin layer chromatography results confirmed that monosaccharide, disaccharide and maltotriose are the hydrolysis products. The results of our study suggest that this enzyme has considerable potential in industrial applications.